YFR022W - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001918 YFR022W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001918 YFR022W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ROG3 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VI:196821..199022
+|nowrap| Chr VI:196833..199034
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000001918

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25 {{SGDpaper|S000128206}} PMID 18976803</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20
+'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20 {{SGDpaper|S000052678}} PMID 10958669</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25
-  {{SGDpaper|S000052678}} PMID 10958669</ref>
+  {{SGDpaper|S000128206}} PMID 18976803</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20 {{SGDpaper|S000052678}} PMID 10958669</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25
+'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25 {{SGDpaper|S000128206}} PMID 18976803</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20
-  {{SGDpaper|S000128206}} PMID 18976803</ref>
+  {{SGDpaper|S000052678}} PMID 10958669</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25 {{SGDpaper|S000128206}} PMID 18976803</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20
+'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20 {{SGDpaper|S000052678}} PMID 10958669</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000128206'>Lin CH, et al. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135(4):714-25
-  {{SGDpaper|S000052678}} PMID 10958669</ref>
+  {{SGDpaper|S000128206}} PMID 18976803</ref>
 <br>
 <br>

@@ Line 8: / Line 8: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ROG3 ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||'' ''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''ART7''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFR022W:''' Protein that binds to Rsp5p, which is a hect-type ubiquitin ligase, via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant<ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20
+'''Description of YFR022W:''' Protein that binds the ubiquitin ligase Rsp5p via its 2 PY motifs; has similarity to Rod1p; mutation suppresses the temperature sensitivity of an mck1 rim11 double mutant; proposed to regulate the endocytosis of plasma membrane proteins<ref name='S000128206'>Lin CH, et al. (2008) Arrestin-Related Ubiquitin-Ligase Adaptors Regulate Endocytosis and Protein Turnover at the Cell Surface. Cell  {{SGDpaper|S000128206}} PMID 18976803</ref><ref name='S000070307'>Andoh T, et al. (2002) PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance. FEBS Lett 525(1-3):131-4 {{SGDpaper|S000070307}} PMID 12163175</ref><ref name='S000052678'>Andoh T, et al. (2000) Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Mol Cell Biol 20(18):6712-20
   {{SGDpaper|S000052678}} PMID 10958669</ref>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
		+	J Biol Chem 278(5):3265-74</ref>
		+	-->

	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr VI:196821..199022
 |}
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 ==Community Commentary==
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